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. 2021 Jul 1;11:13705. doi: 10.1038/s41598-021-91662-w

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Structural implications of the D614G mutation in S-protein. (a) Domain organisation of SARS-CoV-2 nsp12 in complex with nsp7 and nsp8 cofactors. The P323 is depicted in beige spheres. (b) Close up around P323. The residues of the ³²¹FPPTS³²⁵ stretch are depicted in sticks, while F396 that P323 interacts with is depicted in spheres. (c) Residues P116, P183 and R190 of the nsp8 that has been reported to be crucial for the nsp8/nsp12 interaction in SAR-CoV-1 are depicted in red spheres.